JP3353503B2 - Food adhesive - Google Patents
Food adhesiveInfo
- Publication number
- JP3353503B2 JP3353503B2 JP29297094A JP29297094A JP3353503B2 JP 3353503 B2 JP3353503 B2 JP 3353503B2 JP 29297094 A JP29297094 A JP 29297094A JP 29297094 A JP29297094 A JP 29297094A JP 3353503 B2 JP3353503 B2 JP 3353503B2
- Authority
- JP
- Japan
- Prior art keywords
- adhesive
- food
- transglutaminase
- present
- meat
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 230000001070 adhesive effect Effects 0.000 title claims description 68
- 239000000853 adhesive Substances 0.000 title claims description 64
- 235000013305 food Nutrition 0.000 title claims description 53
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 32
- 108060008539 Transglutaminase Proteins 0.000 claims description 25
- 102000003601 transglutaminase Human genes 0.000 claims description 25
- 239000000463 material Substances 0.000 claims description 19
- 239000000843 powder Substances 0.000 claims description 18
- 235000012239 silicon dioxide Nutrition 0.000 claims description 17
- 239000000377 silicon dioxide Substances 0.000 claims description 15
- 102000004169 proteins and genes Human genes 0.000 claims description 14
- 108090000623 proteins and genes Proteins 0.000 claims description 14
- 239000004480 active ingredient Substances 0.000 claims description 8
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 235000013372 meat Nutrition 0.000 description 22
- 241000251468 Actinopterygii Species 0.000 description 14
- 235000019688 fish Nutrition 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 13
- 230000000694 effects Effects 0.000 description 12
- 239000000796 flavoring agent Substances 0.000 description 10
- 235000019634 flavors Nutrition 0.000 description 10
- 235000015170 shellfish Nutrition 0.000 description 5
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 241000237509 Patinopecten sp. Species 0.000 description 4
- 244000144972 livestock Species 0.000 description 4
- 235000013311 vegetables Nutrition 0.000 description 4
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 3
- 102220547770 Inducible T-cell costimulator_A23L_mutation Human genes 0.000 description 3
- 125000002252 acyl group Chemical group 0.000 description 3
- 239000011575 calcium Substances 0.000 description 3
- 229910052791 calcium Inorganic materials 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 235000013399 edible fruits Nutrition 0.000 description 3
- 235000013601 eggs Nutrition 0.000 description 3
- 230000001771 impaired effect Effects 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 235000015277 pork Nutrition 0.000 description 3
- 235000020637 scallop Nutrition 0.000 description 3
- 235000014102 seafood Nutrition 0.000 description 3
- NEAQRZUHTPSBBM-UHFFFAOYSA-N 2-hydroxy-3,3-dimethyl-7-nitro-4h-isoquinolin-1-one Chemical compound C1=C([N+]([O-])=O)C=C2C(=O)N(O)C(C)(C)CC2=C1 NEAQRZUHTPSBBM-UHFFFAOYSA-N 0.000 description 2
- 241000972773 Aulopiformes Species 0.000 description 2
- 108010076119 Caseins Proteins 0.000 description 2
- 102000011632 Caseins Human genes 0.000 description 2
- 241000238424 Crustacea Species 0.000 description 2
- 241000238557 Decapoda Species 0.000 description 2
- 241000276438 Gadus morhua Species 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108010011756 Milk Proteins Proteins 0.000 description 2
- 102000014171 Milk Proteins Human genes 0.000 description 2
- 241000237852 Mollusca Species 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 210000000845 cartilage Anatomy 0.000 description 2
- 238000013329 compounding Methods 0.000 description 2
- 238000006911 enzymatic reaction Methods 0.000 description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 235000021239 milk protein Nutrition 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 235000019515 salmon Nutrition 0.000 description 2
- RMAQACBXLXPBSY-UHFFFAOYSA-N silicic acid Chemical compound O[Si](O)(O)O RMAQACBXLXPBSY-UHFFFAOYSA-N 0.000 description 2
- 241001223854 teleost fish Species 0.000 description 2
- LDVVTQMJQSCDMK-UHFFFAOYSA-N 1,3-dihydroxypropan-2-yl formate Chemical compound OCC(CO)OC=O LDVVTQMJQSCDMK-UHFFFAOYSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- 241001519451 Abramis brama Species 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 235000002566 Capsicum Nutrition 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 241000238366 Cephalopoda Species 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 241001149724 Cololabis adocetus Species 0.000 description 1
- 239000004278 EU approved seasoning Substances 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- JEFZIKRIDLHOIF-BYPYZUCNSA-N Gln-Gly Chemical compound NC(=O)CC[C@H](N)C(=O)NCC(O)=O JEFZIKRIDLHOIF-BYPYZUCNSA-N 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000033345 Merluccius productus Species 0.000 description 1
- 241000238413 Octopus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 239000006002 Pepper Substances 0.000 description 1
- 235000016761 Piper aduncum Nutrition 0.000 description 1
- 235000017804 Piper guineense Nutrition 0.000 description 1
- 244000203593 Piper nigrum Species 0.000 description 1
- 235000008184 Piper nigrum Nutrition 0.000 description 1
- 241000269908 Platichthys flesus Species 0.000 description 1
- 241000785681 Sander vitreus Species 0.000 description 1
- 241000269851 Sarda sarda Species 0.000 description 1
- 241001125046 Sardina pilchardus Species 0.000 description 1
- 241000269821 Scombridae Species 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241001495137 Streptomyces mobaraensis Species 0.000 description 1
- 235000010724 Wisteria floribunda Nutrition 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 235000015278 beef Nutrition 0.000 description 1
- 108010033929 calcium caseinate Proteins 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 239000000679 carrageenan Substances 0.000 description 1
- 235000010418 carrageenan Nutrition 0.000 description 1
- 229920001525 carrageenan Polymers 0.000 description 1
- 229940113118 carrageenan Drugs 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- PXEDJBXQKAGXNJ-QTNFYWBSSA-L disodium L-glutamate Chemical compound [Na+].[Na+].[O-]C(=O)[C@@H](N)CCC([O-])=O PXEDJBXQKAGXNJ-QTNFYWBSSA-L 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 235000013332 fish product Nutrition 0.000 description 1
- 235000011194 food seasoning agent Nutrition 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 150000004698 iron complex Chemical class 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 238000010030 laminating Methods 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 241000238565 lobster Species 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 235000020640 mackerel Nutrition 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 239000011812 mixed powder Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 235000013923 monosodium glutamate Nutrition 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 235000010987 pectin Nutrition 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 244000144977 poultry Species 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000004576 sand Substances 0.000 description 1
- 235000019512 sardine Nutrition 0.000 description 1
- 238000004513 sizing Methods 0.000 description 1
- 229940080237 sodium caseinate Drugs 0.000 description 1
- 235000002639 sodium chloride Nutrition 0.000 description 1
- 229940073490 sodium glutamate Drugs 0.000 description 1
- 235000019830 sodium polyphosphate Nutrition 0.000 description 1
- 235000019710 soybean protein Nutrition 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 238000009864 tensile test Methods 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 230000008719 thickening Effects 0.000 description 1
- 238000006276 transfer reaction Methods 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 241001446247 uncultured actinomycete Species 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000000230 xanthan gum Substances 0.000 description 1
- 229920001285 xanthan gum Polymers 0.000 description 1
- 235000010493 xanthan gum Nutrition 0.000 description 1
- 229940082509 xanthan gum Drugs 0.000 description 1
- UHVMMEOXYDMDKI-JKYCWFKZSA-L zinc;1-(5-cyanopyridin-2-yl)-3-[(1s,2s)-2-(6-fluoro-2-hydroxy-3-propanoylphenyl)cyclopropyl]urea;diacetate Chemical compound [Zn+2].CC([O-])=O.CC([O-])=O.CCC(=O)C1=CC=C(F)C([C@H]2[C@H](C2)NC(=O)NC=2N=CC(=CC=2)C#N)=C1O UHVMMEOXYDMDKI-JKYCWFKZSA-L 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y203/00—Acyltransferases (2.3)
- C12Y203/02—Aminoacyltransferases (2.3.2)
- C12Y203/02013—Protein-glutamine gamma-glutamyltransferase (2.3.2.13), i.e. transglutaminase or factor XIII
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/04—Animal proteins
- A23J3/08—Dairy proteins
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L13/00—Meat products; Meat meal; Preparation or treatment thereof
- A23L13/03—Coating with a layer; Stuffing, laminating, binding, or compressing of original meat pieces
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof
- A23L17/50—Molluscs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L17/00—Food-from-the-sea products; Fish products; Fish meal; Fish-egg substitutes; Preparation or treatment thereof
- A23L17/75—Coating with a layer, stuffing, laminating, binding or compressing of original fish pieces
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/06—Enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
- A23L29/275—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents of animal origin, e.g. chitin
- A23L29/281—Proteins, e.g. gelatin or collagen
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L29/00—Foods or foodstuffs containing additives; Preparation or treatment thereof
- A23L29/20—Foods or foodstuffs containing additives; Preparation or treatment thereof containing gelling or thickening agents
- A23L29/294—Inorganic additives, e.g. silica
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- Nutrition Science (AREA)
- Food Science & Technology (AREA)
- Zoology (AREA)
- Marine Sciences & Fisheries (AREA)
- Biochemistry (AREA)
- Organic Chemistry (AREA)
- Dispersion Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Genetics & Genomics (AREA)
- Inorganic Chemistry (AREA)
- Wood Science & Technology (AREA)
- General Preparation And Processing Of Foods (AREA)
- Meat, Egg Or Seafood Products (AREA)
- Enzymes And Modification Thereof (AREA)
Description
【0001】[0001]
【産業上の利用分野】本発明は、畜肉、魚介肉、野菜、
果実などの食品を素材(原料)とし、これらを接着加工
して製造される接着食品、例えば、成形魚介、成形肉、
成形野菜、成形果実などの成形食品、を製造する際の食
品用接着剤に関する。The present invention relates to meat, seafood, vegetables,
Foods such as fruits are used as materials (raw materials), and adhesive foods are manufactured by bonding these, such as molded seafood, molded meat,
The present invention relates to a food adhesive for producing molded foods such as molded vegetables and molded fruits.
【0002】[0002]
【従来の技術】従来、例えば畜肉を接着して成形ステー
キを製造する場合、糊剤として大豆蛋白や卵白などの蛋
白素材、カラゲナンやキサンタガムなどのガム類、寒天
やペクチンなどの増粘多糖類などが用いられてきた。し
かしながら、これについては、以下のような問題があ
り、全ての食材に対して性能が高くかつ汎用性のある接
着剤は見いだせていなかった。2. Description of the Related Art Conventionally, for example, when a molded steak is produced by bonding livestock meat, protein materials such as soybean protein and egg white, gums such as carrageenan and xanthan gum, and thickening polysaccharides such as agar and pectin are used as sizing agents. Has been used. However, this has the following problems, and no high-performance and versatile adhesive has been found for all food materials.
【0003】その問題の第一は、接着力が弱いために接
着剤を大量に用いないと接着力が発現しないことであ
る。問題の第二は、被接着物の表面(接着面)に均一に
ムラなく接着剤が付着し難いので接着ムラが起こること
である。問題の第三は、現在用いられている上述の接着
剤は大なり小なりの特有の味と臭いを有しており、特に
被接着物として生鮮素材を用いる場合、得られる接着食
品の味や風味を低下させてしまう。特に、現在の使用さ
れている接着剤は、上述のように、ある程度使用量を多
くしないと接着力がでないため、この味および風味の問
題が重要となっている。[0003] The first problem is that the adhesive force is weak unless the adhesive is used in a large amount because the adhesive force is weak. The second problem is that the adhesive hardly adheres uniformly to the surface (adhesive surface) of the object to be adhered, so that uneven adhesion occurs. The third problem is that the above-mentioned adhesives currently used have a characteristic taste and odor of a greater or lesser degree. It reduces the flavor. In particular, as described above, since the adhesive used at present does not have an adhesive force unless the amount used is increased to some extent, the problem of taste and flavor is important.
【0004】[0004]
【発明が解決しようとする課題】前項記載の従来技術の
背景下に、本発明の目的は、食品素材を接着する際、味
や臭いを改良するために少量で被接着物表面に均一な皮
膜をつくりかつ十分な接着力を発現できる接着剤、換言
すれば、従来から課題であった、接着力がありかつ味や
風味が問題にならない食品用接着剤を提供することにあ
る。SUMMARY OF THE INVENTION Under the background of the prior art described in the preceding paragraph, an object of the present invention is to improve the taste and odor when bonding food materials and to form a uniform film on the surface of the adherend in a small amount to improve the taste and odor. In other words, it is an object of the present invention to provide a food adhesive having an adhesive force and having no problem in taste and flavor, which has conventionally been a problem.
【0005】[0005]
【課題を解決するための手段】前項記載の課題を達成す
るためには、求める接着剤が強力な接着力を有するこ
と、味及び風味の点からは少量使用のために接着したい
食品素材に薄い皮膜を形成し接着面に均一に接着剤がコ
ーティングされることが必要である。Means for Solving the Problems In order to achieve the above-mentioned object, it is necessary that the desired adhesive has a strong adhesive force, and in terms of taste and flavor, it is thin on a food material to be adhered for use in a small amount. It is necessary that a film is formed and the adhesive surface is uniformly coated with the adhesive.
【0006】本発明者は、強力な接着力を得るために蛋
白架橋形成能のあるトランスグルタミナーゼを用い、か
つ粉体の流動性改善を目的として微粒化二酸化珪素に着
目して鋭意検討を重ねた結果、薄層付着コーティングを
可能な技術を案出し、その結果ほとんどの食品素材に対
して接着力を有し、味風味の優れた、かつ接着後の接着
食品が、煮る、焼く、炒める、蒸すなどの一般的な加熱
調理を行なっても接着面の剥離することがない食品用接
着剤を見いだし、本発明を完成するに至った。因みに、
トランスグルタミナーゼ及び蛋白を有効成分とする食品
用接着剤は既に知られているが(例えば、欧州特許出願
公開第0572987号)、これに微粒化二酸化珪素を
併用した例は未だ知られていない。[0006] The present inventors have conducted intensive studies by using transglutaminase capable of forming a protein crosslink to obtain a strong adhesive force and focusing on finely divided silicon dioxide for the purpose of improving the fluidity of powder. As a result, we have devised a technology that enables thin-layer adhesion coating, and as a result, it has adhesiveness to most food materials, and has excellent flavor and flavor, and the bonded food after bonding can be boiled, baked, fried, steamed The present inventors have found an adhesive for food that does not peel off the adhesive surface even when general heating cooking is performed, and have completed the present invention. By the way,
Food glues containing transglutaminase and a protein as active ingredients are already known (for example, EP-A-0572987), but no examples have been known in which micronized silicon dioxide is used in combination therewith.
【0007】すなわち、本発明は、第一に、有効成分と
してトランスグルタミナーゼ、蛋白粉末および微粒化二
酸化珪素を含有することを特徴とする食品用接着剤に関
する。That is, the present invention firstly relates to a food adhesive characterized by containing transglutaminase, protein powder and finely divided silicon dioxide as active ingredients.
【0008】以下、本発明を詳細に説明する。Hereinafter, the present invention will be described in detail.
【0009】本発明の食品用接着剤による接着加工の対
象となる食品素材(原料)としては、畜肉、魚肉、貝、
卵、野菜、果実等動植物の食品素材全てを挙げることが
できる。例えば、畜肉でいえば、牛肉、豚肉、鷄肉、魚
肉、羊肉、山羊肉、家禽肉などであり、特に種類及び部
位は限定されない。また、これらを2種以上組合せて用
いてもさしつかえない。魚介類でいえば、硬骨魚類、軟
骨魚類などの魚類のみならず、甲殻類、軟体動物、貝
類、魚卵類も挙げることができる。例えば、スケトウタ
ラ、さんま、あじ、いわし、かつお、さけ、ハモ、鯛、
したびらめ、かれい、ホキ、シログチ、イトヨリ、パシ
フィックホワイティングなどの硬骨魚類、さめ、えいな
どの軟骨魚類、エビ、カニ、ロブスターなどの甲殻類、
いか、たこなどの軟体動物、ほたて、あわびなどの貝類
等であり、特に魚種に限定されるものではない。また、
部位限定されず、更に、2種以上を組み合わせて用いて
も良いことは、畜肉の場合と同様である。The food material (raw material) to be subjected to the bonding process using the food adhesive of the present invention includes livestock meat, fish meat, shellfish,
Examples include all animal and plant food materials such as eggs, vegetables, and fruits. For example, livestock meat includes beef, pork, chicken, fish, sheep, goat, poultry, and the like, and the type and site are not particularly limited. Also, two or more of these may be used in combination. Speaking of seafood, not only fish such as teleost fish and cartilage fish, but also crustaceans, mollusks, shellfish, and fish eggs can be mentioned. For example, walleye cod, saury, mackerel, sardine, bonito, salmon, harmo, bream,
Teleost fish such as turtlefish, shrimp, hoki, shiroguchi, Itoyori, Pacific whiting, cartilage fish such as shark, sei, crustaceans such as shrimp, crab, lobster,
They are mollusks such as squid, octopus and shellfish such as scallop and abalone, and are not particularly limited to fish species. Also,
It is the same as the case of animal meat that two or more kinds may be used in combination without being limited.
【0010】本発明の食品用接着剤の有効成分の1つで
あり、しかも従来本発明の属する技術分野においては利
用されたことのなかった微粒化二酸化珪素について、先
ず説明する。First, the atomized silicon dioxide, which is one of the active ingredients of the food adhesive of the present invention and has not been used in the technical field to which the present invention belongs, will be described first.
【0011】本発明において用いられる微粒化二酸化珪
素とは、粉体の流動性改善作用を有し、かつ、本発明の
食品用接着剤を使用して製造された接着食品を食する際
に砂粒感などの異物感を生じない粒度の二酸化珪素を言
う。The finely divided silicon dioxide used in the present invention refers to a powder having an effect of improving the fluidity of powder and having a grain size of sand when eating an adhesive food produced using the food adhesive of the present invention. This refers to silicon dioxide having a particle size that does not cause a foreign object feeling such as a feeling.
【0012】このような二酸化珪素としては、例えば、
「サイロページ」という商品名で富士シリヒア化学
(株)より販売されている無水珪酸の微粉末を挙げるこ
とができる。また、この二酸化珪素微粉末は固結防止用
として米国食品医薬品局(FDA)により、その使用が
許可されている。この無水珪酸の微粉末は、成分はSi
O2 を99%以上含有し、粒度はミクロンサイズで、通
常は2〜5ミクロン程度のものを指す。微粉化二酸化珪
素の、食品用接着剤の総量に対する配合比率は0.1〜
4%、好ましくは1〜3%である。これが0.1%以下
であると添加効果がみられず、一方、4%以上では効果
が一定となり、配合比率をこれ以上あげる意味がない。As such silicon dioxide, for example,
A fine powder of anhydrous silicic acid sold by Fuji Sirihia Chemical Co., Ltd. under the trade name "Silopage" can be mentioned. The use of this fine silicon dioxide powder has been approved by the US Food and Drug Administration (FDA) to prevent caking. This fine powder of silicic acid is composed of Si
O 2 and contained 99% or more, a particle size in the micron size, generally refers to one of 2 to 5 microns. The mixing ratio of the finely divided silicon dioxide to the total amount of the food adhesive is 0.1 to
4%, preferably 1-3%. If the content is less than 0.1%, the effect of addition is not observed, while if it is more than 4%, the effect is constant and there is no point in increasing the mixing ratio further.
【0013】次に、他の有効成分である蛋白粉末につい
て説明する。この蛋白粉末は、トランスグルタミナーゼ
との相互作用において、少量で強い接着作用を発揮する
ことを目的として使用される。Next, a protein powder as another active ingredient will be described. This protein powder is used for the purpose of exhibiting a strong adhesive action with a small amount in the interaction with transglutaminase.
【0014】このような蛋白粉末としては、乳蛋白が好
ましい。乳蛋白とは、粉乳、カゼイン、カゼインナトリ
ウム、カゼインカルシウムなどの乳より調製されるもの
であれば、いずれでもよい。蛋白粉末の、食品用接着剤
の総量に対する配合比率は30〜90%であり、70%
程度が接着力と付着量の両面からも最も好ましい条件と
いえる。この配合比率が30%以下の時は添加効果がみ
られず、一方、90%以上では薄層付着が困難になり、
ダマ的な付着状態となって好ましくない。As such a protein powder, milk protein is preferable. The milk protein may be any protein prepared from milk, such as milk powder, casein, sodium caseinate and calcium caseinate. The mixing ratio of the protein powder to the total amount of the food adhesive is 30 to 90%,
The degree is the most preferable condition in terms of both the adhesive strength and the amount of adhesion. When the compounding ratio is 30% or less, the effect of addition is not seen, while when it is 90% or more, thin layer adhesion becomes difficult,
It is not preferable because it becomes a sticky state.
【0015】最後に、残りの有効成分であるトランスグ
ルタミナーゼについて説明する。Finally, the remaining active ingredient, transglutaminase, will be described.
【0016】トランスグルタミナーゼには、周知のよう
に、カルシウム非依存性のものとカルシウム依存性のも
のとがある。前者の例としては、微生物由来のもの(例
えば、特開平1−27471参照)を挙げることができ
る。後者の例としては、モルモット肝臓由来のもの(特
公平1−50382参照)、魚由来のもの(例えば、関
信夫ら「日本水産学会誌」56巻1号125頁(199
0))などを挙げることができる。この他、遺伝子組み
換えにより製造されるもの(特開平1−300889、
同5−199883号、同6−225775号等参照)
を挙げることができる。本発明の食品用接着剤には、い
ずれのトランスグルタミナーゼでも用いることができ、
起源及び製法に制限されるところはない。ただし、機能
性及び経済性の点から、好ましくはカルシウム非依存性
のものがよい。例えば、上述の微生物由来のトランスグ
ルタミナーゼ(前掲特開平1−27471)は、いずれ
の条件をも満足するものであり、現時点では最適といえ
る。As is well known, transglutaminase includes calcium-independent and calcium-dependent ones. Examples of the former include those derived from microorganisms (for example, see JP-A-1-27471). Examples of the latter include those derived from guinea pig liver (see Japanese Patent Publication No. 1-50382) and those derived from fish (for example, Nobuo Seki et al., "Journal of the Japanese Society of Fisheries Science", Vol. 56, No. 1, page 125 (199).
0)). In addition, those produced by genetic recombination (JP-A-1-300889,
5-199883, 6-225775, etc.)
Can be mentioned. For the food adhesive of the present invention, any transglutaminase can be used,
There is no restriction on the origin and the manufacturing method. However, from the viewpoints of functionality and economy, a calcium-independent one is preferred. For example, the above-mentioned microorganism-derived transglutaminase (the above-mentioned Japanese Patent Application Laid-Open No. 1-27471) satisfies all the conditions, and can be said to be optimal at present.
【0017】トランスグルタミナーゼの本発明の食品用
接着剤における配合比率については、食品用接着剤1g
当り1〜500ユニット、好ましくは20〜100ユニ
ットとなるように配合すればよい。この添加量が1ユニ
ット以下ではトランスグルタミナーゼ無添加のコントロ
ールと接着力の点で余り変わらず、一方、500ユニッ
ト以上では接着速度が速すぎて作業性が悪くなるからで
ある。この食品用接着剤を肉等の被接着物に対して均一
になるようにまぶせばよい。The mixing ratio of transglutaminase in the food adhesive of the present invention is as follows.
The amount may be 1 to 500 units, preferably 20 to 100 units per unit. If the amount is less than 1 unit, the adhesive strength is not much different from that of the control without transglutaminase, while if the amount is more than 500 units, the adhesive speed is too high and the workability is deteriorated. What is necessary is just to apply | coat this food adhesive so that it may become even with respect to an adherend, such as meat.
【0018】さて、被接着物に対する本発明の食品用接
着剤の付着率を約0.7g/100cm2 程度と想定す
ると、被接着物の接着面の単位面積(100cm2 )当
りのトランスグルタミナーゼの量は0.7〜350ユニ
ット程度になるものと考えられる。もちろん、この被接
着物当りのトランスグルタミナーゼの量は一応の目安で
あり、これに拘わるものではない。Assuming that the adhesion rate of the food adhesive of the present invention to the adherend is about 0.7 g / 100 cm 2, the amount of transglutaminase per unit area (100 cm 2 ) of the adhered surface of the adherend can be improved. It is believed that the amount will be on the order of 0.7 to 350 units. Of course, the amount of transglutaminase per adherend is only a rough guide and is not limited to this.
【0019】因みに、本発明に関して言うトランスグル
タミナーゼの活性単位は、次のようにして測定され、か
つ定義される。すなわち、ベンジルオキシカルボニル−
L−グルタミニルグリシンとヒドロキシルアミンを基質
として反応を行い、生成したヒドロキサム酸をトリクロ
ル酢酸存在下で鉄錯体を形成させた後、525nmの吸
光度を測定し、ヒドロキサム酸の量を検量線より求め、
活性を算出する(前掲特開平1−27471号公報参
照)。Incidentally, the activity unit of transglutaminase referred to in the present invention is measured and defined as follows. That is, benzyloxycarbonyl-
A reaction was performed using L-glutaminylglycine and hydroxylamine as substrates, and the resulting hydroxamic acid was allowed to form an iron complex in the presence of trichloroacetic acid. Thereafter, the absorbance at 525 nm was measured, and the amount of hydroxamic acid was determined from a calibration curve.
The activity is calculated (see the above-mentioned JP-A-1-27471).
【0020】本発明の食品用接着剤には、接着作用を呈
する有効成分としての、上に説明した微粒化二酸化珪
素、蛋白粉末およびトランスグルタミナーゼの他に、こ
れらの成分の接着作用を妨げない限度において、乳糖、
ポリリン酸ナトリウムなどの補助剤、塩、こしょう、グ
ルタミン酸ナトリウム、砂糖、蛋白加水分解物などの調
味料、レシチン、モノグリセリドなどの乳化剤、その他
を所望により賦形剤を兼ねて添加配合することのできる
ことは言うまでもない。In the food adhesive of the present invention, in addition to the above-mentioned finely divided silicon dioxide, protein powder and transglutaminase as active ingredients having an adhesive action, the adhesive action of these ingredients is not impaired. In, lactose,
Additives such as sodium polyphosphate, salt, pepper, seasonings such as sodium glutamate, sugar, protein hydrolyzate, emulsifiers such as lecithin, monoglyceride, etc. Needless to say.
【0021】これら成分をそれぞれ適当量採って本発明
の食品用接着剤を調製するには特別の困難はなにもな
く、単なる粉体混合によることができる。There are no particular difficulties in preparing the food adhesive of the present invention by taking appropriate amounts of each of these components, and it is possible to simply mix the powder.
【0022】このようにして調製した食品用接着剤は、
直ちに食品素材の接着に使用することのできることはも
ちろんであり、また食品用接着剤として流通に置くこと
のできることも言うまでもない。The food adhesive thus prepared is
Needless to say, it can be used immediately for bonding food materials, and it can be put on the market as a food adhesive.
【0023】本発明は、第二は、上に説明した、有効成
分としてトランスグルタミナーゼ、蛋白粉末および微粒
化二酸化珪素を含有する食品用接着剤を使用して食品素
材を接着することを特徴とする接着食品の製造方法に関
する。The second aspect of the present invention is characterized in that a food material is adhered using the above-mentioned food adhesive containing transglutaminase, protein powder and finely divided silicon dioxide as active ingredients. The present invention relates to a method for producing an adhesive food.
【0024】以下、この製造方法について、詳細に例示
説明する。Hereinafter, this manufacturing method will be described in detail by way of example.
【0025】まず、トランスグルタミナーゼ粉末、蛋白
粉末および微粒化二酸化珪素ならびに所望により配合す
る添加物を各所定量計量し、円錐型スクリュー混合機や
ニーダーなどを用いて混合する。First, a predetermined amount of each of the transglutaminase powder, the protein powder, the finely divided silicon dioxide, and the additives to be blended is weighed and mixed using a conical screw mixer or a kneader.
【0026】この混合粉末を、例えば、トレイに5mm
程度の厚さに敷き詰める。この状態の粉末の上に被接着
食品素材を軽く置く。つぎに、食品素材の反対の面を同
様の方法で処理する。このようにして得られた数枚の、
食品用接着剤の粉付着処理食品素材を、例えば、ケーシ
ングチューブに充填するとか、型箱に積層させて形成す
る。The mixed powder is placed on a tray, for example, by 5 mm.
Spread to the desired thickness. The adhered food material is lightly placed on the powder in this state. Next, the opposite side of the food material is treated in a similar manner. Several pieces obtained in this way,
The powdery food material of the food adhesive is applied, for example, by filling a casing tube or by laminating a mold box.
【0027】この接着成形物を目的に応じて所定の温度
条件下で所定の時間処理して接着させる。This adhesive molded article is treated and adhered under a predetermined temperature condition for a predetermined time according to the purpose, and is adhered.
【0028】周知のように、トランスグルタミナーゼ
は、ペプチド鎖内にあるグルタミン残基のγ−カルボキ
シアミド基のアシル転移反応を触媒する酵素である。こ
のトランスグルタミナーゼは、アシル受容体としてタン
パク質中のリジン残基のε−アミノ基が作用すると、タ
ンパク質分子の分子内において及び分子間においてε−
(γ−Glu)−Lys架橋結合が形成される。また、
水がアシル受容体として機能するときは、グルタミン残
基が脱アミド化されてグルタミン酸残基になる反応を進
行させる酵素である。As is well known, transglutaminase is an enzyme that catalyzes an acyl transfer reaction of the γ-carboxamide group of a glutamine residue in a peptide chain. This transglutaminase, when the ε-amino group of a lysine residue in a protein acts as an acyl receptor, ε-
A (γ-Glu) -Lys crosslink is formed. Also,
When water functions as an acyl acceptor, it is an enzyme that promotes a reaction in which a glutamine residue is deamidated into a glutamic acid residue.
【0029】本発明においては、このようなトランスグ
ルタミナーゼの酵素作用を活用するので、上に言う所定
の温度および所定の時間はトランスグルタミナーゼの
(至適)作用条件を考慮して定める。すなわち、本発明
の食品素材の接着のためのトランスグルタミナーゼの酵
素反応の条件は、温度は0℃以上であるが、余り高温に
なると酵素が失活するため、一般的には0〜60℃であ
る。ただし、製造時に速やかに処理したときは20〜4
0℃で処理するとよいが、生鮮食品素材である畜肉や魚
介類の加工処理の場合は、0〜5℃くらいの温度で処理
した方が素材の鮮度が良く保たれるので好ましい。ま
た、反応時間は、反応温度よって異なるが、通常5分〜
15時間である。In the present invention, since the above-mentioned enzyme action of transglutaminase is utilized, the above-mentioned predetermined temperature and predetermined time are determined in consideration of the (optimum) action conditions of transglutaminase. That is, the conditions of the enzymatic reaction of transglutaminase for adhesion of the food material of the present invention are such that the temperature is 0 ° C. or higher, but when the temperature is too high, the enzyme is inactivated. is there. However, when processed promptly during manufacture, 20 to 4
The treatment is preferably performed at 0 ° C., but in the case of processing meat, fish and shellfish, which are fresh food materials, it is preferable to perform the treatment at a temperature of about 0 to 5 ° C. because the freshness of the material can be maintained well. The reaction time varies depending on the reaction temperature, but is usually from 5 minutes to
15 hours.
【0030】このようにしての、本発明の食品用接着剤
を使用する接着処理を経た処理物(接着食品)は、例え
ばそのまま生のままでまたは加熱してから必要に応じ適
当な大きさに例えば包丁で成形して流通に置くことがで
きる。また、このものは、魚であれば生のまま刺身とし
てや焼き物、煮物、フライ物などとして食することがで
きる。また、このものが畜肉であれば、ステーキやフラ
イ物として食することができる。The treated product (adhesive food) which has been subjected to the adhesive treatment using the food adhesive of the present invention in this manner is, for example, neat or heated, and then, if necessary, to an appropriate size. For example, it can be molded with a kitchen knife and placed in distribution. In addition, this fish can be eaten raw as raw fish, grilled, boiled, fried or the like. If the meat is meat, it can be eaten as a steak or fried food.
【0031】[0031]
【実施例】以下、実施例によって本発明を更に詳しく説
明する。本発明の技術的範囲は、もちろん、これによっ
て規定されるものではない。The present invention will be described in more detail with reference to the following examples. The technical scope of the present invention is, of course, not limited thereby.
【0032】実施例1(接着剤) 食品用接着剤5種類を下記第1表に示すレシピー(a)
〜(e)に従って配合することにより調製して微粒化二
酸化珪素の効果を確認した。なお、トランスグルタミナ
ーゼは、放線菌ストレプトベルチシリウムに属する微生
物(Streptoverticillium mobaraense IFO 13819)起源
のトランスグルタミナーゼ(比活性1ユニット/mg)
を使用した。Example 1 (Adhesive) Five types of food adhesives were used as recipes (a) shown in Table 1 below.
To (e) to confirm the effect of finely divided silicon dioxide. In addition, transglutaminase is a transglutaminase derived from a microorganism belonging to the actinomycete Streptoverticillium (Streptoverticillium mobaraense IFO 13819) (specific activity 1 unit / mg).
It was used.
【0033】[0033]
【表1】 [Table 1]
【0034】これらの接着剤を、それぞれ、トレーに一
定厚み以上に入れた。その上に一定断面積(約100c
m2 )にスライスした豚ロース肉を置いた。この時付着
した接着剤の重量(g)を測定し、単位面積(100c
m2 )当りに換算して付着率とした(g/100c
m2 )。同時に肉表面の均一付着性を観察した。Each of these adhesives was put in a tray to a certain thickness or more. A constant cross-sectional area (approx.
m 2 ) was placed with sliced pork loin. The weight (g) of the adhesive adhered at this time was measured, and the unit area (100 c
m 2) was adhered ratio in terms of per (g / 100c
m 2 ). At the same time, uniform adhesion on the meat surface was observed.
【0035】その結果、付着率は、接着剤レシピ(a)
0.83、(b)0.72、(c)0.66、(d)
0.66、そして(e)0.65であった。この数値は
低い方が好ましい。何故なら、より少ない量で均一に付
着されるからである。さて、この結果から、微粒化二酸
化珪素の配合比率は、2%までは付着物が改善されるが
それ以上では効果が変わらないことがわかった。同時に
行なった肉に対する均一付着性の観察結果は、無添加の
ものは肉表面にぼてぼてと不均一に付着していたが、添
加品は滑らかに均一に付着していた。そのとき、2%ま
での効果が大きかったが、それ以上では差が殆どわから
なかった。As a result, the adhesion ratio is determined by the adhesive recipe (a).
0.83, (b) 0.72, (c) 0.66, (d)
0.66 and (e) 0.65. This value is preferably low. This is because a smaller amount is uniformly applied. From this result, it was found that the content of the finely divided silicon dioxide was improved up to 2%, but the effect was not changed at higher than 2%. At the same time, the results of observation of uniform adhesion to meat showed that the non-added ones were unevenly adhered to the meat surface, but the added products were smoothly and uniformly attached. At that time, the effect was large up to 2%, but above that, the difference was hardly noticeable.
【0036】以上のことから、微粒化二酸化珪素の配合
比率は、この場合は、2%程度が効果の点からも、経済
的な点からも適当であることがわかった。From the above, it was found that, in this case, the compounding ratio of the atomized silicon dioxide is about 2%, which is appropriate from the viewpoint of the effect and the economical viewpoint.
【0037】実施例2(畜肉の接着) 実施例1に示す接着剤のレシピのうち、最も付着量が改
善され、経済的なものとした第1表のレシピ(c)を選
定し、その接着強度を測定した。Example 2 (Adhesion of Meat) Among the adhesive recipes shown in Example 1, recipe (c) in Table 1 was selected, which was the most economical one in which the adhesion amount was improved, and the adhesion was selected. The strength was measured.
【0038】すなわち、豚股肉の小片(2cm角程度)
の表面に該接着剤を均一にまぶし(付着させ)、これを
折幅75mmのケーシングに充填結紮し、そのまま室温
に約2時間放置してトランスグルタミナーゼによる酵素
反応を行なった後、−40℃の冷凍庫で一夜保存した。
それを半解凍状態で厚さ9mm、幅25mmにスライス
カットし、更に完全解凍させた直後に不動工業(株)製
レオメーターによる引張試験を行った。その結果120
g/cm2 の強い接着強度を示した。That is, a piece of pork crotch (about 2 cm square)
The adhesive was evenly spread on (adhered to) the surface of the sample, and this was filled and ligated in a casing having a folded width of 75 mm, and allowed to stand at room temperature for about 2 hours to carry out an enzymatic reaction with transglutaminase. Stored in the freezer overnight.
It was slice-cut in a half-thaw state to a thickness of 9 mm and a width of 25 mm. Immediately after the slice was completely thawed, a tensile test was performed with a rheometer manufactured by Fudo Kogyo Co., Ltd. As a result 120
g / cm 2 .
【0039】このものは同時に、10〜12mm厚さの
ステーキ状にスライスし、グリル試験を行った結果、非
常に良く接着しており、かつ風味的にも肉本来の味及び
風味を全く損なうことなく一枚肉同様の品質を保持して
いた。This product was sliced at the same time into a steak shape having a thickness of 10 to 12 mm, and as a result of a grill test, it was found to be very well adhered, and that the taste and flavor of the meat were completely impaired. But kept the same quality as one piece of meat.
【0040】実施例3(魚肉の接着) サワラの切身(7×3×2cm程度)を約1000g用
意し、実施例2で使用したと同じレシピの接着剤をトレ
ーに入れ、切身の1枚1枚に接着剤を均一にまぶし、リ
テーナーに空隙の無い様に積み重ね圧着した。そのもの
を室温に2時間程度放置後凍結し、一夜保持した。Example 3 (Adhesion of Fish Meat) Approximately 1000 g of soybean fillet (approximately 7 × 3 × 2 cm) was prepared, and an adhesive having the same recipe as used in Example 2 was placed in a tray. The adhesive was evenly applied to the sheets, and the sheets were stacked and pressure-bonded to the retainer without any voids. It was allowed to stand at room temperature for about 2 hours, then frozen and kept overnight.
【0041】これを解凍後約10〜15mm厚さにスラ
イスした時、生の状態でも良く接着しており、かつそれ
をグリル調理したも全くはがれることなく、一枚の切身
をグリルした時と同じ品質を有していた。また、その
味、風味も全く損われることがなかった。また、このス
ライス品に衣をつけて170〜180℃でフライするこ
とにより魚フライ品を得た。このものも、一枚の切身を
フライしたものと同様の品質を有していた。When this is sliced to a thickness of about 10 to 15 mm after thawing, it is well adhered even in a raw state, and it is grilled and does not come off at all. Had quality. The taste and flavor were not impaired at all. A fried fish product was obtained by putting a batter on this sliced product and frying it at 170 to 180 ° C. This also had the same quality as a single fried piece.
【0042】また、この接着剤は、タラ、サケ、ヒラメ
などの魚肉に対しても同様の効果が有った。This adhesive had the same effect on fish meat such as cod, salmon and flounder.
【0043】実施例4(貝肉の接着) 生のホタテ貝柱を約500g用意し、前実施例における
と同じレシピの接着剤をトレーにいれ、これを一個一個
の貝柱に均一にまぶした後、折径120mmのファイブ
ラスケーシングに詰め結紮し、室温に約2時間放置した
後、−40℃の冷凍庫で一夜保持した。Example 4 (Adhesion of shell meat) About 500 g of raw scallop scallop was prepared, an adhesive having the same recipe as in the previous example was placed in a tray, and this was uniformly spread on each scallop. The pieces were packed and ligated in a fibrous casing having a folded diameter of 120 mm, left at room temperature for about 2 hours, and then kept in a freezer at -40 ° C overnight.
【0044】このものを半解凍後、約1.0〜1.3m
mにスライスした時、生の状態でも良く接着しており、
更にそれをグリルしたときも全くはがれることなく、ま
た全くその味及び風味を損なうことなく、一枚のホタテ
ステーキ様の品質を有していた。After this is half-thawed, it is about 1.0 to 1.3 m
When sliced into m, it adheres well even in the raw state,
Furthermore, when grilled, it had a quality of one scallop steak without peeling off at all and without impairing its taste and flavor.
【0045】[0045]
【発明の効果】本発明によれば、畜肉、魚肉、貝、魚、
卵、野菜などの食品素材を接着する際に食品素材の接着
表面に薄層に付着し、少量の接着剤量にて強力な接着作
用を示し、かつ味及び風味の優れた接着食品が提供され
る。According to the present invention, livestock meat, fish meat, shellfish, fish,
When bonding food materials such as eggs and vegetables, it adheres to a thin layer on the bonding surface of the food material, shows a strong adhesive action with a small amount of adhesive, and provides an adhesive food with excellent taste and flavor You.
───────────────────────────────────────────────────── フロントページの続き (58)調査した分野(Int.Cl.7,DB名) A23L 1/00 - 1/03 A23J 3/08 A23L 1/325 A23L 1/31 ──────────────────────────────────────────────────続 き Continued on the front page (58) Field surveyed (Int. Cl. 7 , DB name) A23L 1/00-1/03 A23J 3/08 A23L 1/325 A23L 1/31
Claims (3)
ゼ、蛋白粉末および微粒化二酸化珪素を含有することを
特徴とする食品用接着剤。1. An adhesive for foods comprising as active ingredients transglutaminase, protein powder and finely divided silicon dioxide.
食品素材を接着することを特徴とする接着食品の製造方
法。2. A method for producing an adhesive food, comprising bonding a food material using the food adhesive according to claim 1.
り製造されたことを特徴とする接着食品。3. An adhesive food product produced by the method for producing an adhesive food product according to claim 2.
Priority Applications (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP29297094A JP3353503B2 (en) | 1994-11-28 | 1994-11-28 | Food adhesive |
| EP95118643A EP0713651B1 (en) | 1994-11-28 | 1995-11-27 | Food adhesive |
| DE69519916T DE69519916T2 (en) | 1994-11-28 | 1995-11-27 | Binders for food |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP29297094A JP3353503B2 (en) | 1994-11-28 | 1994-11-28 | Food adhesive |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH08140594A JPH08140594A (en) | 1996-06-04 |
| JP3353503B2 true JP3353503B2 (en) | 2002-12-03 |
Family
ID=17788789
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP29297094A Expired - Lifetime JP3353503B2 (en) | 1994-11-28 | 1994-11-28 | Food adhesive |
Country Status (3)
| Country | Link |
|---|---|
| EP (1) | EP0713651B1 (en) |
| JP (1) | JP3353503B2 (en) |
| DE (1) | DE69519916T2 (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008120798A1 (en) | 2007-03-29 | 2008-10-09 | Ajinomoto Co., Inc. | Enzyme preparation for adhesion and method of producing adhesion-molded food product |
| WO2010035856A1 (en) | 2008-09-25 | 2010-04-01 | 味の素株式会社 | Enzyme preparation for adhesion-molded foods and method for producing adhesion-molded food |
Families Citing this family (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3407599B2 (en) * | 1996-07-01 | 2003-05-19 | 味の素株式会社 | Enzyme preparation for adhesion and method for producing adhesive food |
| JP3706945B2 (en) * | 1997-04-28 | 2005-10-19 | カネボウ株式会社 | Molded food |
| JP2981612B1 (en) * | 1998-06-25 | 1999-11-22 | 亮一 深江 | Rice shower aggregates |
| DE19840744A1 (en) * | 1998-09-07 | 2000-03-09 | Zimbo Fleisch Und Wurstwaren G | Production of low-fat meat products such as sausages by mincing mixture of lean meat, water, pickling salt and ballasting material and treating with transaminase |
| DE19939226A1 (en) * | 1999-08-18 | 2001-03-01 | Kemper Gmbh & Co H | Preparation of fried meat-on-a-bone fast food to be held in the hand for consumption, assembles pieces of meat onto e.g. denatured bone |
| KR100377812B1 (en) * | 2000-07-10 | 2003-03-26 | 김영찬 | A production method of mixing meat for having multiple taste |
| ATE453323T1 (en) * | 2002-08-02 | 2010-01-15 | Ajinomoto Kk | BINDER FOR MEAT AND SEAFOOD AND METHOD FOR PRODUCING FOOD SHAPED WITH THE BINDER |
| KR100638354B1 (en) * | 2005-01-27 | 2006-10-24 | 주식회사 엠이에이상사 | How to Make Tteokgalbi |
| JP6787563B2 (en) * | 2016-06-30 | 2020-11-18 | 千葉製粉株式会社 | Manufacturing method of adhesive molded food, adhesive component dispersion liquid for adhesive molded food, and adhesive molded food |
| JP6780379B2 (en) * | 2016-08-30 | 2020-11-04 | 味の素株式会社 | Manufacturing method of processed meat food |
| CN106942459B (en) * | 2017-03-08 | 2018-06-19 | 苏州欧福蛋业股份有限公司 | The preparation and application of a kind of high glue protein powder of superelevation degree of gelation for noodles |
| US11102998B1 (en) | 2017-08-25 | 2021-08-31 | The Hershey Company | Binders and methods of making and using the same |
| KR102874268B1 (en) * | 2024-11-19 | 2025-10-21 | 주식회사 티에스푸드 | Method for manufacturing vegetable roll tempura and vegetable roll tempura manufactured thereby |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH0665280B2 (en) * | 1987-03-04 | 1994-08-24 | 味の素株式会社 | Protein gelling agent and protein gelling method using the same |
| JPH0673440B2 (en) * | 1991-10-25 | 1994-09-21 | 三蔵 真能 | Vacuum packaged food |
| EP0572987B1 (en) * | 1992-06-02 | 1999-08-25 | Ajinomoto Co., Inc. | Process for producing bound-formed food |
-
1994
- 1994-11-28 JP JP29297094A patent/JP3353503B2/en not_active Expired - Lifetime
-
1995
- 1995-11-27 EP EP95118643A patent/EP0713651B1/en not_active Expired - Lifetime
- 1995-11-27 DE DE69519916T patent/DE69519916T2/en not_active Expired - Lifetime
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2008120798A1 (en) | 2007-03-29 | 2008-10-09 | Ajinomoto Co., Inc. | Enzyme preparation for adhesion and method of producing adhesion-molded food product |
| WO2010035856A1 (en) | 2008-09-25 | 2010-04-01 | 味の素株式会社 | Enzyme preparation for adhesion-molded foods and method for producing adhesion-molded food |
| US8192770B2 (en) | 2008-09-25 | 2012-06-05 | Ajinomoto Co., Inc. | Enzyme preparation for adhesion-molded foods and method for producing adhesion-molded food |
Also Published As
| Publication number | Publication date |
|---|---|
| DE69519916D1 (en) | 2001-02-22 |
| DE69519916T2 (en) | 2001-08-02 |
| JPH08140594A (en) | 1996-06-04 |
| EP0713651A1 (en) | 1996-05-29 |
| EP0713651B1 (en) | 2001-01-17 |
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